PMID:11827487
| Citation |
Lima, CD (2002) Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation. J. Mol. Biol. 315:1199-208 |
|---|---|
| Abstract |
The Escherichia coli NifS CsdB protein is a member of the homodimeric pyridoxal 5'-phosphate (PLP)-dependent family of enzymes. These enzymes are capable of decomposing cysteine or selenocysteine into L-alanine and sulfur or selenium, respectively. E. coli NifS CsdB has a high specificity for L-selenocysteine in comparison to l-cysteine, suggesting a role for this enzyme is selenium metabolism. The 2.0 A crystal structure of E. coli NifS CsdB reveals a high-resolution view of the active site of this enzyme in apo-, persulfide, perselenide, and selenocysteine-bound intermediates, suggesting a mechanism for the stabilization of the enzyme persulfide and perselenide intermediates during catalysis, a necessary intermediate in the formation of sulfur and selenium containing metabolites. |
| Links |
PubMed Online version:10.1006/jmbi.2001.5308 |
| Keywords |
Apoenzymes/chemistry; Apoenzymes/genetics; Apoenzymes/metabolism; Bacillus subtilis/enzymology; Bacillus subtilis/genetics; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Binding Sites; Crystallography, X-Ray; Cysteine/analogs & derivatives; Cysteine/metabolism; Disulfides/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Ligands; Lyases/chemistry; Lyases/genetics; Lyases/metabolism; Models, Molecular; Organoselenium Compounds/metabolism; Protein Conformation; Selenocysteine/metabolism; Structure-Activity Relationship; Sulfides/metabolism; Thermodynamics |
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